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. 1973 May;52(5):1276–1281. doi: 10.1172/JCI107295

Structural Identity of Bence Jones and Amyloid Fibril Proteins in a Patient with Plasma Cell Dyscrasia and Amyloidosis

William D Terry 1,2, David L Page 1,2, Shigeru Kimura 1,2, Takashi Isobe 1,2, Elliott F Osserman 1,2, George G Glenner 1,2
PMCID: PMC302384  PMID: 4700495

Abstract

The partial amino acid sequence of the amyloid fibril protein isolated from the small intestine of a patient with plasma cell dyscrasia and associated amyloidosis has been determined and compared with the sequence of the κ-type Bence Jones protein isolated from the urine of the same patient. Identical sequences were observed for the 27 amino-terminal residues that could be compared. The C-terminal tryptic peptide of the amyloid protein was identical with that of the Bence Jones protein. Apparent molecular weights and amino acid compositions of the Bence Jones and amyloid proteins were similar. It appears, therefore, that the predominant protein present in the amyloid deposits in this patient was an intact κ-type light polypeptide chain that was identical with the urinary Bence Jones protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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